Modulation of the redox state of quinones by light in Rhodobacter sphaeroides under anaerobic conditions

• Published in: Photosynthesis research 2014-05, Vol.120 (1-2), p.237-246
• Main Authors: Verméglio, André, Joliot, Pierre
• Format: Article
• Language: English
• Subjects: anaerobic conditions; Anaerobiosis; Biochemistry; Biomedical and Life Sciences; chromatophores; Electron transfer; Electron transport; Fluorescence; Life Sciences; Light; lighting; oxidation; Oxidation-Reduction - radiation effects; Photochemistry; Photosynthesis; Plant Genetics and Genomics; Plant Physiology; Plant Sciences; Quinone; quinones; Regular Paper; Rhodobacter sphaeroides; Rhodobacter sphaeroides - metabolism; Rhodobacter sphaeroides - radiation effects
• ISSN: 0166-8595; 1573-5079
• DOI: 10.1007/s11120-013-9961-8

Illumination of intact cells of Rhodobacter sphaeroides under anaerobic conditions has a dual effect on the redox state of the quinone pool. A large oxidation of the quinone pool is observed during the first seconds following the illumination. This oxidation is suppressed by the addition of an uncoupler in agreement with a light-induced reverse electron transfer at the level of the complex I, present both in the non-invaginated part of the membrane and in the chromatophores. At longer dark times, this illumination increases the reducing power of the cells leading to a significant reduction of the others reaction centers (RCs). From the observation that a significant proportion of RCs could be reduced by the preillumination without affecting the numbers of charge separation for the RCs, we conclude that there is no rapid thermodynamic equilibrium between the quinones present in the non-invaginated part of the membrane and those localized in the chromatophores. Under anaerobic conditions where the chromatophores quinone pool is fully reduced, we deduce, on the basis of flash-induced fluorescence kinetics, that the reduced RCs are exclusively reoxidized by the quinone generated at the Q ₒ site of the cyt bc ₁ complex. The supramolecular association between a dimeric RC-LHI complex and one cyt bc ₁ complex allows the confinement of a quinone between the RC-LHI directly associated to the cyt bc ₁ complex.